Structure of PDB 6fba Chain B

Receptor sequence
>6fbaB (length=317) Species: 5833 (Plasmodium falciparum) [Search protein sequence]
DLDKIMTKMKNKSVINIDDVDDEELLAILYTSKQFEKILKNNEDSKYLEN
KVFCSVFLEPSTRTRCSFDAAILKLGSKVLNITDMNSTSFYKGETVEDAF
KILSTYVDGIIYRDPSKKNVDIAVSSSSKPIINAGNGTGEHPTQSLLDFY
TIHNYFPFILDRNINKKLNIAFVGDLKNGRTVHSLSKLLSRYNVSFNFVS
CKSLNIPKDIVNTITYNLKKNNFYSDDSIKYFDNLEEGLEDVHIIYMTRI
QYNQYKNAFILSNKTLENTRDDTKILHPLPRVNEIKVEVDSNPKSVYFTQ
AENGLYVRMALLYLIFS
3D structure
PDB6fba Identification of a non-competitive inhibitor of Plasmodium falciparum aspartate transcarbamoylase.
ChainB
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R109 T110 K138 R159 H187 Q190 T294 P333 G359
Catalytic site (residue number reindexed from 1) R63 T64 K92 R113 H141 Q144 T248 P278 G304
Enzyme Commision number 2.1.3.2: aspartate carbamoyltransferase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 D48 B R109 P335 R63 P280 MOAD: Kd=19.9uM
PDBbind-CN: -logKd/Ki=4.70,Kd=19.9uM
BS02 D48 B E140 I148 L149 Y152 E94 I102 L103 Y106 MOAD: Kd=19.9uM
PDBbind-CN: -logKd/Ki=4.70,Kd=19.9uM
Gene Ontology
Molecular Function
GO:0004070 aspartate carbamoyltransferase activity
GO:0016597 amino acid binding
GO:0016740 transferase activity
GO:0016743 carboxyl- or carbamoyltransferase activity
Biological Process
GO:0006207 'de novo' pyrimidine nucleobase biosynthetic process
GO:0006221 pyrimidine nucleotide biosynthetic process
GO:0006520 amino acid metabolic process
GO:0044205 'de novo' UMP biosynthetic process
Cellular Component
GO:0016020 membrane

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Cellular Component
External links
PDB RCSB:6fba, PDBe:6fba, PDBj:6fba
PDBsum6fba
PubMed29476738
UniProtO15804

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